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Conserved domains on  [gi|518903407|ref|WP_020059282|]
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cytochrome c oxidase subunit I [Bacillus sp. 123MFChir2]

Protein Classification

cytochrome c oxidase subunit I( domain architecture ID 10108844)

cytochrome c oxidase subunit I is a heme-copper oxygen reductase, located in the mitochondrial inner membrane or the bacterial inner cell membrane, which catalyzes the reduction of molecular oxygen to water and is typically the terminal electron acceptor

CATH:  1.20.210.10
EC:  7.1.1.9
Gene Ontology:  GO:0046872|GO:0020037|GO:0015990|GO:0004129
PubMed:  35630371
SCOP:  4001989

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 17-514 0e+00

Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


:

Pssm-ID: 238832  Cd Length: 501  Bit Score: 778.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVFAMMNAAVPLQ 96
Cdd:cd01662    1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  97 IGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLSLA--SKGHGIDFYVLGLQISGIGTLIGGINFLV 174
Cdd:cd01662   81 IGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLeySPGVGVDYWILGLQFSGIGTLLGAINFIV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 175 TIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYIL 254
Cdd:cd01662  161 TILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYIL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 255 ILPVFGIFSEIFATFSKKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLFTM 334
Cdd:cd01662  241 ILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTM 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 335 WGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKILDE 414
Cdd:cd01662  321 WRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNE 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 415 TLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQGLETGNLISSIGAAFMALGTIVLLVNVVKTS-FSKKQAGR 493
Cdd:cd01662  401 RLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIrKGKRDATG 480

                        490       500
                 ....*....|....*....|.
gi 518903407 494 DPWDGRTLEWAIPAPTPEYNF 514
Cdd:cd01662  481 DPWGARTLEWATSSPPPAYNF 501
 
Name Accession Description Interval E-value
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 17-514 0e+00

Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238832  Cd Length: 501  Bit Score: 778.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVFAMMNAAVPLQ 96
Cdd:cd01662    1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  97 IGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLSLA--SKGHGIDFYVLGLQISGIGTLIGGINFLV 174
Cdd:cd01662   81 IGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLeySPGVGVDYWILGLQFSGIGTLLGAINFIV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 175 TIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYIL 254
Cdd:cd01662  161 TILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYIL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 255 ILPVFGIFSEIFATFSKKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLFTM 334
Cdd:cd01662  241 ILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTM 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 335 WGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKILDE 414
Cdd:cd01662  321 WRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNE 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 415 TLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQGLETGNLISSIGAAFMALGTIVLLVNVVKTS-FSKKQAGR 493
Cdd:cd01662  401 RLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIrKGKRDATG 480

                        490       500
                 ....*....|....*....|.
gi 518903407 494 DPWDGRTLEWAIPAPTPEYNF 514
Cdd:cd01662  481 DPWGARTLEWATSSPPPAYNF 501
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
11-541 0e+00

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 772.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  11 GSVIWDYLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVFAMMN 90
Cdd:COG0843    3 GSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGFGN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  91 AAVPLQIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLSL--ASKGHGIDFYVLGLQISGIGTLIG 168
Cdd:COG0843   83 YLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGleASPGVGVDLWLLGLALFGVGSILG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 169 GINFLVTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGH 248
Cdd:COG0843  163 GVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 249 PEVYILILPVFGIFSEIFATFSKKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIF 328
Cdd:COG0843  243 PEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVF 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 329 NWLFTMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMF 408
Cdd:COG0843  323 NWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMT 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 409 NKILDETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQGLETGNLISSIGAAFMALGTIVLLVNVVKTSFSK 488
Cdd:COG0843  403 GRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKG 482

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 518903407 489 KQAGRDPWDGRTLEWAIPAPTPEYNFKQLPFVRGLDPLWIEKREGKDEITPAE 541
Cdd:COG0843  483 PKAGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE 535
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 18-514 0e+00

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 674.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407   18 LTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVFAMMNAAVPLQI 97
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLPLMI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407   98 GARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLSLA--SKGHGIDFYVLGLQISGIGTLIGGINFLVT 175
Cdd:TIGR02891  81 GARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTsgSPGVGVDLWLLGLHLLGISSILGAVNFIVT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  176 IINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYILI 255
Cdd:TIGR02891 161 ILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  256 LPVFGIFSEIFATFSKKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLFTMW 335
Cdd:TIGR02891 241 LPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  336 GGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKILDET 415
Cdd:TIGR02891 321 GGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNER 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  416 LGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQGLETGNLISSIGAAFMALGTIVLLVNVVKTSFSKKQAGRDP 495
Cdd:TIGR02891 401 LGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANP 480

                         490
                  ....*....|....*....
gi 518903407  496 WDGRTLEWAIPAPTPEYNF 514
Cdd:TIGR02891 481 WGATTLEWTTSSPPPAHNF 499
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 9-602 1.78e-172

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 506.01  E-value: 1.78e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407   9 GVGSVIW-DYLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNND---FLVGDAYNQVLTMHGTTMIFLAAMPL 84
Cdd:PRK15017  39 GKWTYLWkEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGeagFLPPHHYDQIFTAHGVIMIFFVAMPF 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  85 VFAMMNAAVPLQIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLSLA--SKGHGIDFYVLGLQISG 162
Cdd:PRK15017 119 VIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIeySPGVGVDYWIWSLQLSG 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 163 IGTLIGGINFLVTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHL 242
Cdd:PRK15017 199 IGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINL 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 243 FWIFGHPEVYILILPVFGIFSEIFATFSKKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVP 322
Cdd:PRK15017 279 IWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIP 358

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 323 TGIKIFNWLFTMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHY 402
Cdd:PRK15017 359 TGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTY 438

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 403 YWPLMFNKILDETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQgLETGNLISSIGAAFMALGTIVLLVNV- 481
Cdd:PRK15017 439 WWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQ-FHTMLMIAASGAALIALGILCQVIQMy 517

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 482 --VKTSFSKKQAGRDPWDGRTLEWAIPAPTPEYNFKQLPFVRGLDPLWIEKREGKDEITPAEpIGDIHMPNASflpfviS 559
Cdd:PRK15017 518 vsIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGEAYKQPDH-YEEIHMPKNS------G 590

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*
gi 518903407 560 LGLFIAAFGAMYMQGGKEKMW--LVVAIVGLIITFGAMFFRSVID 602
Cdd:PRK15017 591 AGIVIAAFSTIFGFAMIWHIWwlAIVGFAGMIITWIVKSFDEDVD 635
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 25-469 4.72e-158

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 460.50  E-value: 4.72e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407   25 KIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVFAMMNAAVPLQIGARDVAF 104
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  105 PFLNSLGFWLFFFGGVFLNLSWflgGAPDAGWTSYASLSlaskghGIDFYVLGLQISGIGTLIGGINFLVTIINMRAPGM 184
Cdd:pfam00115  81 PRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLV------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  185 TyMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGtsffnpALGGNTIIWEHLFWIFGHPEVYILILPVFGIFSE 264
Cdd:pfam00115 152 T-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYY 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  265 IFATFSKKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLFTMWGGSIRF-TT 343
Cdd:pfam00115 225 ILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTT 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  344 PMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKILDETLGKITFWL 423
Cdd:pfam00115 305 PMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWL 384

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 518903407  424 FFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQ--GLETGNLISSIGAAF 469
Cdd:pfam00115 385 LFIGFNLTFFPMHILGLLGMPRRYAPPFIETvpAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 17-514 0e+00

Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238832  Cd Length: 501  Bit Score: 778.68  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVFAMMNAAVPLQ 96
Cdd:cd01662    1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  97 IGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLSLA--SKGHGIDFYVLGLQISGIGTLIGGINFLV 174
Cdd:cd01662   81 IGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLeySPGVGVDYWILGLQFSGIGTLLGAINFIV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 175 TIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYIL 254
Cdd:cd01662  161 TILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYIL 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 255 ILPVFGIFSEIFATFSKKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLFTM 334
Cdd:cd01662  241 ILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTM 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 335 WGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKILDE 414
Cdd:cd01662  321 WRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNE 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 415 TLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQGLETGNLISSIGAAFMALGTIVLLVNVVKTS-FSKKQAGR 493
Cdd:cd01662  401 RLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIrKGKRDATG 480

                        490       500
                 ....*....|....*....|.
gi 518903407 494 DPWDGRTLEWAIPAPTPEYNF 514
Cdd:cd01662  481 DPWGARTLEWATSSPPPAYNF 501
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
11-541 0e+00

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 772.76  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  11 GSVIWDYLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVFAMMN 90
Cdd:COG0843    3 GSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGFGN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  91 AAVPLQIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLSL--ASKGHGIDFYVLGLQISGIGTLIG 168
Cdd:COG0843   83 YLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGleASPGVGVDLWLLGLALFGVGSILG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 169 GINFLVTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGH 248
Cdd:COG0843  163 GVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGH 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 249 PEVYILILPVFGIFSEIFATFSKKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIF 328
Cdd:COG0843  243 PEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVF 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 329 NWLFTMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMF 408
Cdd:COG0843  323 NWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMT 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 409 NKILDETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQGLETGNLISSIGAAFMALGTIVLLVNVVKTSFSK 488
Cdd:COG0843  403 GRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKG 482

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|...
gi 518903407 489 KQAGRDPWDGRTLEWAIPAPTPEYNFKQLPFVRGLDPLWIEKREGKDEITPAE 541
Cdd:COG0843  483 PKAGGNPWGARTLEWATPSPPPLYNFASIPVVRSRDPAYDYKKPGADFVPPAE 535
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 18-514 0e+00

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 674.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407   18 LTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVFAMMNAAVPLQI 97
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLPLMI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407   98 GARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLSLA--SKGHGIDFYVLGLQISGIGTLIGGINFLVT 175
Cdd:TIGR02891  81 GARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTsgSPGVGVDLWLLGLHLLGISSILGAVNFIVT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  176 IINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYILI 255
Cdd:TIGR02891 161 ILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  256 LPVFGIFSEIFATFSKKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLFTMW 335
Cdd:TIGR02891 241 LPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  336 GGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKILDET 415
Cdd:TIGR02891 321 GGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNER 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  416 LGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQGLETGNLISSIGAAFMALGTIVLLVNVVKTSFSKKQAGRDP 495
Cdd:TIGR02891 401 LGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQMGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANP 480

                         490
                  ....*....|....*....
gi 518903407  496 WDGRTLEWAIPAPTPEYNF 514
Cdd:TIGR02891 481 WGATTLEWTTSSPPPAHNF 499
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 16-613 0e+00

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 663.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407   16 DYLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVFAMMNAAVPL 95
Cdd:TIGR02882  43 EWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIGLMNIVVPL 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407   96 QIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLSLA--SKGHGIDFYVLGLQISGIGTLIGGINFL 173
Cdd:TIGR02882 123 QIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPefSPGVGVNYYLIALQISGIGTLMTGINFF 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  174 VTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYI 253
Cdd:TIGR02882 203 VTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYI 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  254 LILPVFGIFSEIFATFSKKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLFT 333
Cdd:TIGR02882 283 VILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLT 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  334 MWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKILD 413
Cdd:TIGR02882 363 LYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLN 442

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  414 ETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQGLETGNLISSIGAAFMALGTIVLLVNVVKTSF-SKKQAG 492
Cdd:TIGR02882 443 ERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYSPSDGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRkSPREAT 522

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  493 RDPWDGRTLEWAIPAPTPEYNFKQLPFVRGLDPLWIEKREGKDEITPAEPIGDIHMPNASFLPFVISLGLFIAAFGAMYm 572
Cdd:TIGR02882 523 GDPWNGRTLEWATASPPPKYNFAVTPDVNDYDAFWDMKKHGYRHYLDNENYKDIHMPNNSGVGFWIGIFFFIGGFFLVF- 601

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 518903407  573 qggkekMWLVVAIVGLIITFGAMFFRSVIDDHGYHIHKEDL 613
Cdd:TIGR02882 602 ------ETVAPAIVGAFGIFGTLIYRSFEIDDGYHIPAAEI 636
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 23-484 0e+00

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 558.30  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  23 HKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVFAMMNAAVPLQIGARDV 102
Cdd:cd00919    1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGARDL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 103 AFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLSL--ASKGHGIDFYVLGLQISGIGTLIGGINFLVTIINMR 180
Cdd:cd00919   81 AFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTlsYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 181 APGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYILILPVFG 260
Cdd:cd00919  161 APGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFG 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 261 IFSEIFATFSKKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLFTMWGGSIR 340
Cdd:cd00919  241 AISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIR 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 341 FTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKILDETLGKIT 420
Cdd:cd00919  321 FDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIH 400

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518903407 421 FWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPgqGLETGNLISSIGAAFMALGTIVLLVNVVKT 484
Cdd:cd00919  401 FWLWFIGFNLTFFPMHFLGLLGMPRRYADYPD--GFAPWNFISSVGAFILGLGLLLFLGNLFLS 462
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 22-505 0e+00

Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 548.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  22 DHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVF-AMMNAAVPLQIGAR 100
Cdd:cd01663    2 NHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIgGFGNWLVPLMIGAP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 101 DVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGINFLVTIIN 178
Cdd:cd01663   82 DMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSsiLAHSGPSVDLAIFSLHLAGISSILGAINFITTIFN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 179 MRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYILILPV 258
Cdd:cd01663  162 MRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPG 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 259 FGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLFTMWGG 337
Cdd:cd01663  242 FGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGG 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 338 SIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKILDETLG 417
Cdd:cd01663  322 SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 418 KITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYlPGQgLETGNLISSIGAAFMALGTIVLLVNVVKTSFSKKQAGRDPWD 497
Cdd:cd01663  402 KIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDY-PDA-YAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGE 479


                 ....*....
gi 518903407 498 GRT-LEWAI 505
Cdd:cd01663  480 GSTsLEWTL 488
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 9-602 1.78e-172

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 506.01  E-value: 1.78e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407   9 GVGSVIW-DYLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNND---FLVGDAYNQVLTMHGTTMIFLAAMPL 84
Cdd:PRK15017  39 GKWTYLWkEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGeagFLPPHHYDQIFTAHGVIMIFFVAMPF 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  85 VFAMMNAAVPLQIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLSLA--SKGHGIDFYVLGLQISG 162
Cdd:PRK15017 119 VIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIeySPGVGVDYWIWSLQLSG 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 163 IGTLIGGINFLVTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHL 242
Cdd:PRK15017 199 IGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINL 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 243 FWIFGHPEVYILILPVFGIFSEIFATFSKKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVP 322
Cdd:PRK15017 279 IWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIP 358

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 323 TGIKIFNWLFTMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHY 402
Cdd:PRK15017 359 TGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTY 438

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 403 YWPLMFNKILDETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQgLETGNLISSIGAAFMALGTIVLLVNV- 481
Cdd:PRK15017 439 WWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQ-FHTMLMIAASGAALIALGILCQVIQMy 517

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 482 --VKTSFSKKQAGRDPWDGRTLEWAIPAPTPEYNFKQLPFVRGLDPLWIEKREGKDEITPAEpIGDIHMPNASflpfviS 559
Cdd:PRK15017 518 vsIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGEAYKQPDH-YEEIHMPKNS------G 590

                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*
gi 518903407 560 LGLFIAAFGAMYMQGGKEKMW--LVVAIVGLIITFGAMFFRSVID 602
Cdd:PRK15017 591 AGIVIAAFSTIFGFAMIWHIWwlAIVGFAGMIITWIVKSFDEDVD 635
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 25-469 4.72e-158

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 460.50  E-value: 4.72e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407   25 KIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVFAMMNAAVPLQIGARDVAF 104
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  105 PFLNSLGFWLFFFGGVFLNLSWflgGAPDAGWTSYASLSlaskghGIDFYVLGLQISGIGTLIGGINFLVTIINMRAPGM 184
Cdd:pfam00115  81 PRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLV------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  185 TyMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGtsffnpALGGNTIIWEHLFWIFGHPEVYILILPVFGIFSE 264
Cdd:pfam00115 152 T-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYY 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  265 IFATFSKKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLFTMWGGSIRF-TT 343
Cdd:pfam00115 225 ILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTT 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  344 PMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKILDETLGKITFWL 423
Cdd:pfam00115 305 PMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWL 384

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 518903407  424 FFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQ--GLETGNLISSIGAAF 469
Cdd:pfam00115 385 LFIGFNLTFFPMHILGLLGMPRRYAPPFIETvpAFQPLNWIRTIGGVL 432
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 17-521 6.39e-144

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 427.09  E-value: 6.39e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVF-AMMNAAVPL 95
Cdd:MTH00223   3 WLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIgGFGNWLVPL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  96 QIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGINFL 173
Cdd:MTH00223  83 MLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSsnLAHAGPSVDLAIFSLHLAGVSSILGAINFI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 174 VTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYI 253
Cdd:MTH00223 163 TTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 254 LILPVFGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLF 332
Cdd:MTH00223 243 LILPGFGMISHIVSHYSsKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 333 TMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKIL 412
Cdd:MTH00223 323 TIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTL 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 413 DETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYlpGQGLETGNLISSIGAAFMALGTIVLLVNVVKTSFSKKQAG 492
Cdd:MTH00223 403 HRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDY--PDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVV 480

                        490       500
                 ....*....|....*....|....*....
gi 518903407 493 RDPWDGRTLEWAIPAPTPEYNFKQLPFVR 521
Cdd:MTH00223 481 WSGHLSTSLEWDNLLPADFHNNSETGALV 509
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 17-520 9.19e-144

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 426.79  E-value: 9.19e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVFAMM-NAAVPL 95
Cdd:MTH00167   6 WLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFgNWLVPL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  96 QIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGINFL 173
Cdd:MTH00167  86 MIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAgnLAHAGASVDLAIFSLHLAGVSSILGSINFI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 174 VTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYI 253
Cdd:MTH00167 166 TTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 254 LILPVFGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLF 332
Cdd:MTH00167 246 LILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 333 TMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKIL 412
Cdd:MTH00167 326 TLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTL 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 413 DETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYlpGQGLETGNLISSIGAAFMALGTIVLLVNVVKTSFSKKQAG 492
Cdd:MTH00167 406 NETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLL 483

                        490       500
                 ....*....|....*....|....*...
gi 518903407 493 RDPWDGRTLEWAIPAPTPEYNFKQLPFV 520
Cdd:MTH00167 484 PVELTSTNVEWLHGCPPPHHTWEEPPFV 511
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 23-520 5.68e-143

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 424.67  E-value: 5.68e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  23 HKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNdfLVGD--AYNQVLTMHGTTMIFLAAMPLV---FAmmNAAVPLQI 97
Cdd:MTH00153  10 HKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGS--LIGDdqIYNVIVTAHAFIMIFFMVMPIMiggFG--NWLVPLML 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  98 GARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGINFLVT 175
Cdd:MTH00153  86 GAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSsnIAHSGASVDLAIFSLHLAGISSILGAINFITT 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 176 IINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYILI 255
Cdd:MTH00153 166 IINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 256 LPVFGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLFTM 334
Cdd:MTH00153 246 LPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATL 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 335 WGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKILDE 414
Cdd:MTH00153 326 HGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNP 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 415 TLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLpgQGLETGNLISSIGAAFMALGTIVLLVNVVKTSFSKKQAGRD 494
Cdd:MTH00153 406 KWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFS 483

                        490       500
                 ....*....|....*....|....*.
gi 518903407 495 PWDGRTLEWAIPAPTPEYNFKQLPFV 520
Cdd:MTH00153 484 LNLSSSIEWLQNLPPAEHSYSELPLL 509
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 17-520 1.82e-142

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 423.73  E-value: 1.82e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNndFLVGD--AYNQVLTMHGTTMIFLAAMPLVFAMM-NAAV 93
Cdd:MTH00116   6 WLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPG--TLLGDdqIYNVIVTAHAFVMIFFMVMPIMIGGFgNWLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  94 PLQIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGIN 171
Cdd:MTH00116  84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAgnLAHAGASVDLAIFSLHLAGVSSILGAIN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 172 FLVTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEV 251
Cdd:MTH00116 164 FITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 252 YILILPVFGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNW 330
Cdd:MTH00116 244 YILILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSW 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 331 LFTMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNK 410
Cdd:MTH00116 324 LATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGY 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 411 ILDETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYlpGQGLETGNLISSIGAAFMALGTIVLLVnVVKTSFSKKQ 490
Cdd:MTH00116 404 TLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTISSIGSLISMTAVIMLMF-IIWEAFSSKR 480

                        490       500       510
                 ....*....|....*....|....*....|.
gi 518903407 491 AGRDPWDGRT-LEWAIPAPTPEYNFKQLPFV 520
Cdd:MTH00116 481 KVLQPELTTTnIEWIHGCPPPYHTFEEPAFV 511
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 17-516 4.04e-139

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 414.85  E-value: 4.04e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMP-LVFAMMNAAVPL 95
Cdd:MTH00079   7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPsMIGGFGNWMLPL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  96 QIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS-LASKGHGIDFYVLGLQISGIGTLIGGINFLV 174
Cdd:MTH00079  87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLStLGHPGSSVDLAIFSLHCAGISSILGGINFMV 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 175 TIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYIL 254
Cdd:MTH00079 167 TTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYIL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 255 ILPVFGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLFT 333
Cdd:MTH00079 247 ILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLAT 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 334 MWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKILD 413
Cdd:MTH00079 327 LFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYD 406

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 414 ETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLpgQGLETGNLISSIGAAFMALGTIVLLVNVVKTSFSKKQAGR 493
Cdd:MTH00079 407 KLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYP--DVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLH 484

                        490       500
                 ....*....|....*....|...
gi 518903407 494 DPWDGRTLEWAIPAPTPEYNFKQ 516
Cdd:MTH00079 485 DNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 17-518 1.43e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 400.64  E-value: 1.43e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNdfLVGD--AYNQVLTMHGTTMIFLAAMP-LVFAMMNAAV 93
Cdd:MTH00142   4 WLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGS--LLGDdqLYNVIVTAHAFVMIFFMVMPvMIGGFGNWLV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  94 PLQIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGIN 171
Cdd:MTH00142  82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSsnLAHSGGSVDLAIFSLHLAGVSSILGAIN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 172 FLVTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEV 251
Cdd:MTH00142 162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 252 YILILPVFGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNW 330
Cdd:MTH00142 242 YILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 331 LFTMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNK 410
Cdd:MTH00142 322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGL 401

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 411 ILDETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYlpGQGLETGNLISSIGAAFMALGTIVLLVNVVKTSFSKKQ 490
Cdd:MTH00142 402 TLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRL 479

                        490       500
                 ....*....|....*....|....*...
gi 518903407 491 AGRDPWDGRTLEWAIPAPTPEYNFKQLP 518
Cdd:MTH00142 480 VMWSSHLSTSLEWSHRLPPDFHTYDELP 507
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 17-520 2.95e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 400.36  E-value: 2.95e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMP-LVFAMMNAAVPL 95
Cdd:MTH00184   8 WLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPvMIGGFGNWFVPL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  96 QIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGINFL 173
Cdd:MTH00184  88 YIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSsiQAHSGGSVDMAIFSLHLAGISSILGAMNFI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 174 VTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYI 253
Cdd:MTH00184 168 TTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 254 LILPVFGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLF 332
Cdd:MTH00184 248 LILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIA 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 333 TMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKIL 412
Cdd:MTH00184 328 TIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCY 407

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 413 DETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYlpGQGLETGNLISSIGAAFMALGTIVLLVNVVKTSFSKKQA- 491
Cdd:MTH00184 408 NEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDF--HDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFv 485

                        490       500       510
                 ....*....|....*....|....*....|.
gi 518903407 492 --GRDPWDGRTLEWAIPAPTPEYNFKQLPFV 520
Cdd:MTH00184 486 gwVEDSGHYPSLEWAQTSPPAHHTYNELPYV 516
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 17-523 2.27e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 390.34  E-value: 2.27e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMP-LVFAMMNAAVPL 95
Cdd:MTH00182   8 WVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPvMIGGFGNWLVPL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  96 QIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGINFL 173
Cdd:MTH00182  88 YIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSsiQAHSGGAVDMAIFSLHLAGVSSILGAINFI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 174 VTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYI 253
Cdd:MTH00182 168 TTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYI 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 254 LILPVFGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLF 332
Cdd:MTH00182 248 LILPGFGMISQIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 333 TMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKIL 412
Cdd:MTH00182 328 TIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCY 407

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 413 DETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYlpGQGLETGNLISSIGAAFMALGTIVLLVNVVKTSFSKKQ-- 490
Cdd:MTH00182 408 NELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDF--ADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKfi 485

                        490       500       510
                 ....*....|....*....|....*....|....*
gi 518903407 491 --AGRDPWDGRTLEWAIPAPTPEYNFKQLPFVRGL 523
Cdd:MTH00182 486 gwKEGTGESWASLEWVHSSPPLFHTYNELPFVYKS 520
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 17-521 5.17e-129

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 389.24  E-value: 5.17e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNdfLVGD--AYNQVLTMHGTTMIFLAAMPLVFAMM-NAAV 93
Cdd:MTH00103   6 WLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGT--LLGDdqIYNVIVTAHAFVMIFFMVMPIMIGGFgNWLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  94 PLQIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGIN 171
Cdd:MTH00103  84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAgnLAHAGASVDLTIFSLHLAGVSSILGAIN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 172 FLVTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEV 251
Cdd:MTH00103 164 FITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 252 YILILPVFGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNW 330
Cdd:MTH00103 244 YILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 331 LFTMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNK 410
Cdd:MTH00103 324 LATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGY 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 411 ILDETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYlpGQGLETGNLISSIGaAFMALGTIVLLVNVVKTSF-SKK 489
Cdd:MTH00103 404 TLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDY--PDAYTTWNTVSSMG-SFISLTAVMLMIFMIWEAFaSKR 480

                        490       500       510
                 ....*....|....*....|....*....|..
gi 518903407 490 QAGRDPWDGRTLEWAIPAPTPEYNFKQLPFVR 521
Cdd:MTH00103 481 EVLTVELTTTNLEWLHGCPPPYHTFEEPTYVK 512
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 17-521 5.18e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 389.28  E-value: 5.18e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNdfLVGD--AYNQVLTMHGTTMIFLAAMPLVFAMM-NAAV 93
Cdd:MTH00183   6 WFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGA--LLGDdqIYNVIVTAHAFVMIFFMVMPIMIGGFgNWLI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  94 PLQIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGIN 171
Cdd:MTH00183  84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAgnLAHAGASVDLTIFSLHLAGVSSILGAIN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 172 FLVTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEV 251
Cdd:MTH00183 164 FITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 252 YILILPVFGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNW 330
Cdd:MTH00183 244 YILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 331 LFTMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNK 410
Cdd:MTH00183 324 LATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGY 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 411 ILDETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQGLetGNLISSIGAAFMALGTIVLLVNVVKTSFSKKQ 490
Cdd:MTH00183 404 TLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTL--WNTVSSIGSLISLVAVIMFLFILWEAFAAKRE 481

                        490       500       510
                 ....*....|....*....|....*....|.
gi 518903407 491 AGRDPWDGRTLEWAIPAPTPEYNFKQLPFVR 521
Cdd:MTH00183 482 VLSVELTSTNVEWLHGCPPPYHTFEEPAFVQ 512
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 17-520 1.58e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 385.45  E-value: 1.58e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNdfLVGD--AYNQVLTMHGTTMIFLAAMP-LVFAMMNAAV 93
Cdd:MTH00077   6 WLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGT--LLGDdqIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  94 PLQIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGIN 171
Cdd:MTH00077  84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAgnLAHAGASVDLTIFSLHLAGVSSILGAIN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 172 FLVTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEV 251
Cdd:MTH00077 164 FITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEV 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 252 YILILPVFGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNW 330
Cdd:MTH00077 244 YILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSW 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 331 LFTMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNK 410
Cdd:MTH00077 324 LATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGY 403

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 411 ILDETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQGLetGNLISSIGaAFMALGTIVLLVNVVKTSFSKKQ 490
Cdd:MTH00077 404 TLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTL--WNTVSSIG-SLISLVAVIMMMFIIWEAFSSKR 480

                        490       500       510
                 ....*....|....*....|....*....|.
gi 518903407 491 AGRDPWDGRT-LEWAIPAPTPEYNFKQLPFV 520
Cdd:MTH00077 481 EVLTTELTSTnIEWLHGCPPPYHTFEEPSFV 511
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 17-520 4.91e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 379.17  E-value: 4.91e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVFAMM-NAAVPL 95
Cdd:MTH00037   6 WLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFgNWLIPL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  96 QIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGINFL 173
Cdd:MTH00037  86 MIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSsnIAHAGGSVDLAIFSLHLAGASSILASINFI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 174 VTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYI 253
Cdd:MTH00037 166 TTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYI 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 254 LILPVFGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLF 332
Cdd:MTH00037 246 LILPGFGMISHVIAHYSgKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMA 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 333 TMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKIL 412
Cdd:MTH00037 326 TLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSL 405

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 413 DETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYlpGQGLETGNLISSIGAAFMALGTIVLLVNVVKTSFSKKQAG 492
Cdd:MTH00037 406 HPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVI 483

                        490       500
                 ....*....|....*....|....*....
gi 518903407 493 RDPWDGRTLEWAIPA-PTPEYNFKQLPFV 520
Cdd:MTH00037 484 SPEFSSSSLEWQYSSfPPSHHTFDETPST 512
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 17-516 1.03e-119

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 364.99  E-value: 1.03e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMP-LVFAMMNAAVPL 95
Cdd:MTH00007   3 WLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPvFIGGFGNWLVPL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  96 QIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGINFL 173
Cdd:MTH00007  83 MLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLAsnLAHAGPSVDLAIFSLHLAGVSSILGAINFI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 174 VTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYI 253
Cdd:MTH00007 163 TTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 254 LILPVFGIFSEIFATFSKK-RLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLF 332
Cdd:MTH00007 243 LILPGFGAISHIVTHYAGKlEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 333 TMWGGSIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKIL 412
Cdd:MTH00007 323 TIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTL 402

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 413 DETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYlpGQGLETGNLISSIGAAFMALGTIVLLVNVVKTSFSKKQAG 492
Cdd:MTH00007 403 HDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDY--PDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVI 480

                        490       500
                 ....*....|....*....|....
gi 518903407 493 RDPWDGRTLEWAIPAPTPEYNFKQ 516
Cdd:MTH00007 481 ASPHMSSSLEWQDTLPLDFHNLPE 504
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 17-522 5.93e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 348.54  E-value: 5.93e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMP-LVFAMMNAAVPL 95
Cdd:MTH00026   7 WFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPtMIGGFGNWFVPL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  96 QIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGAPDAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGINFL 173
Cdd:MTH00026  87 MIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLAsiQAHSGGSVDMAIFSLHLAGLSSILGAMNFI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 174 VTIINMRAPGMTYMRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYI 253
Cdd:MTH00026 167 TTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 254 LILPVFGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLF 332
Cdd:MTH00026 247 LILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLA 326

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 333 TMWGG--SIRFTTPMIWAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNK 410
Cdd:MTH00026 327 TVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGY 406

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 411 ILDETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYlpGQGLETGNLISSIGAAFMALGTIVLLVNVVKTSFSKKQ 490
Cdd:MTH00026 407 AYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADY--PDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREEP 484

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*
gi 518903407 491 AGRD-------------PWDGRTLEWAIPAPTPEYNFKQLPFVRG 522
Cdd:MTH00026 485 FDINimakgplipfscqPAHFDTLEWSLTSPPEHHTYNELPYIVG 529
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 17-478 1.04e-100

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 315.85  E-value: 1.04e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  17 YLTTVDHKKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMP-LVFAMMNAAVPL 95
Cdd:MTH00048   7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPvLIGGFGNYLLPL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  96 QIGARDVAFPFLNSLGFWLFFFGGVFLNLSWFLGGApdAGWTSYASLS--LASKGHGIDFYVLGLQISGIGTLIGGINFL 173
Cdd:MTH00048  87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAG--VGWTFYPPLSssLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 174 VTIINMRAPGMTYmRMPMFTWTTFVTSALILFAFPPLTVGLALLMLDRLFGTSFFNPALGGNTIIWEHLFWIFGHPEVYI 253
Cdd:MTH00048 165 CTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 254 LILPVFGIFSEIFATFS-KKRLFGYSSMVFATVLIGFLGFMVWAHHMFTVGLGPVANAIFSVATMAIAVPTGIKIFNWLF 332
Cdd:MTH00048 244 LILPGFGIISHICLSLSnNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 333 TMWGGSIRFTTPMI-WAVGFIPSFVMGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAHYYWPLMFNKI 411
Cdd:MTH00048 324 MLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518903407 412 LDETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPgqGLETGNLISSIGAAFMALGTIVLL 478
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEP--SYYWINVVCTVGSFISAFSGCFFV 468
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 24-479 7.28e-33

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 132.02  E-value: 7.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407  24 KKIAILYLIAGGLFFIIGGIEALFIRYQLAFPNNDFLVGDAYNQVLTMHGTTMIFLAAMPLVFAMMNAAVPLQIGARDVA 103
Cdd:cd01660    3 KKLALAHFVVAFLALLLGGLFGLLQVLVRTGVFPLPSSGILYYQGLTLHGVLLAIVFTTFFIMGFFYAIVARALLRSLFN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 104 FPFLNsLGFWLFFFGGVFLNLSWFLGGApDAGWTSYASLslasKGHGidFYVLGLQISGIGTLIGGINFLVTIINMRA-- 181
Cdd:cd01660   83 RRLAW-AGFWLMVIGTVMAAVPILLGQA-SVLYTFYPPL----QAHP--LFYIGAALVVVGSWISGFAMFVTLWRWKKan 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 182 PGMtymRMPMFTWTTFVTSALILFAfpplTVGLALLMLDRLFGTSFFNpALGGNTIIWEHLFWIFGHPEVYILILPVFGI 261
Cdd:cd01660  155 PGK---KVPLATFMVVTTMILWLVA----SLGVALEVLFQLLPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIA 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 262 FSEIFATFSKKRLFGYSSMVFATVLIGFLGFMVWAHHMFT-VGLGPVANAIFSVATMAIAVPT----------------- 323
Cdd:cd01660  227 WYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSlltaftvfasleiagrl 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518903407 324 --GIKIFNWLFTMWGGSIRFTTPMIWAVGFIPsfvmGGVTGVMLASAPADYQFHDNYFVVAHFHYVIVGGVVFGLFAGAH 401
Cdd:cd01660  307 rgGKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAY 382

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518903407 402 YYWPLMFNKIL-DETLGKITFWLFFIGFHLTFFIQHFLGLIGMPRRYFTYLPGQGLETGNLISSigAAFMALGTIVLLV 479
Cdd:cd01660  383 WLVPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTAEAQYGGLPAAGEWAPY--QQLMAIGGTILFV 459
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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